Alzheimer's disease is a neurodegenerative disorder characterized by the extracellular deposition in the brain of aggregated  -amyloid peptide, presumed to play a pathogenic role, and by preferential loss of neurons that express the 75-kD neurotrophin receptor (p75 NTR ). Using rat cortical neurons and NIH-3T3 cell line engineered to stably express p75 NTR , we find that the  -amyloid peptide specifically binds the p75 NTR . Furthermore, 3T3 cells expressing p75 NTR , but not wild-type control cells lacking the receptor, undergo apoptosis in the presence of aggregated  -amyloid. Normal neural crest-derived melanocytes that express physiologic levels of p75 NTR undergo apoptosis in the presence of aggregated  -amyloid, but not in the presence of control peptide synthesized in reverse. These data imply that neuronal death in Alzheimer's disease is mediated, at least in part, by the interaction of  -amyloid with p75 NTR , and suggest new targets for therapeutic intervention. ( J. Clin. Invest. 1997.
The Ash Split catheter allows increased rates of blood flow during hemodialysis but this increase was not significant at the beginning (p = 0.21) or end (p = 0.27) of the first six hemodialysis sessions. The Ash Split catheter is more prone to minor complications, particularly dislodgment, than the PermCath catheter.
We conclude that there are significant histopathologic consequences, focused in the kidney, resulting from the daily administration of high doses of human recombinant TGF-beta2, and we propose that selective vascular constriction with consequent tissue hypoxia is a contributing factor.
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